4IU8

Crystal structure of a membrane transporter (selenomethionine derivative)

4IU8 の概要

• エントリーDOI: 10.2210/pdb4iu8/pdb
• 関連するPDBエントリー: 4IU9
• 分子名称: Nitrite extrusion protein 2, NITRATE ION (2 entities in total)
• 機能のキーワード: membrane protein, nitrate-nitrite porter family transporter, mfs fold, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P37758
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102776.12

構造登録者

Yan, H.,Huang, W.,Yan, C.,Gong, X.,Jiang, S.,Zhao, Y.,Wang, J.,Shi, Y. (登録日: 2013-01-20, 公開日: 2013-04-17, 最終更新日: 2024-11-27)

主引用文献

Yan, H.,Huang, W.,Yan, C.,Gong, X.,Jiang, S.,Zhao, Y.,Wang, J.,Shi, Y.
Structure and mechanism of a nitrate transporter.
Cell Rep, 3:716-723, 2013

PubMed Abstract: The nitrate/nitrite transporters NarK and NarU play an important role in nitrogen homeostasis in bacteria and belong to the nitrate/nitrite porter family (NNP) of the major facilitator superfamily (MFS) fold. The structure and functional mechanism of NarK and NarU remain unknown. Here, we report the crystal structure of NarU at a resolution of 3.1 Å and systematic biochemical characterization. The two molecules of NarU in an asymmetric unit exhibit two distinct conformational states: occluded and partially inward-open. The substrate molecule nitrate appears to be coordinated by four highly conserved, charged, or polar amino acids. Structural and biochemical analyses allowed the identification of key amino acids that are involved in substrate gating and transport. The observed conformational differences of NarU, together with unique sequence features of the NNP family transporters, suggest a transport mechanism that might deviate from the canonical rocker-switch model.

PubMed: 23523348
DOI: 10.1016/j.celrep.2013.03.007

実験手法

X-RAY DIFFRACTION (3.11 Å)